Contribution of the C-terminal end of apolipoprotein AI to neutralization of lipopolysaccharide endotoxic effect

It is well known that high density lipoprotein (HDL) binds bacterial lipopolysaccharide (LPS) and neutralizes its toxicity. The aim of this work was to study changes in the apolipoprotein (apo) AI structure after its interaction with LPS as well as to determine the protein domain involved in that in...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Henning, María Florencia, Herlax, Vanesa Silvana, Bakás, Laura Susana
Formato: Articulo
Lenguaje:Inglés
Publicado: 2011
Materias:
Biología
ANS
ASD-LPS
GdnHCl denaturation
lipoprotein
TNF-alpha
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/83921
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-83921
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Biología
ANS
ASD-LPS
GdnHCl denaturation
lipoprotein
TNF-alpha
spellingShingle Biología
ANS
ASD-LPS
GdnHCl denaturation
lipoprotein
TNF-alpha
Henning, María Florencia
Herlax, Vanesa Silvana
Bakás, Laura Susana
Contribution of the C-terminal end of apolipoprotein AI to neutralization of lipopolysaccharide endotoxic effect
topic_facet Biología
ANS
ASD-LPS
GdnHCl denaturation
lipoprotein
TNF-alpha
description It is well known that high density lipoprotein (HDL) binds bacterial lipopolysaccharide (LPS) and neutralizes its toxicity. The aim of this work was to study changes in the apolipoprotein (apo) AI structure after its interaction with LPS as well as to determine the protein domain involved in that interaction. The presented data indicate that LPS does not lead to major changes in the structure of apoAI, judging from Trp fluorescence spectra. However, analysis of denaturation behavior and binding of ANS show that LPS induces a loosened protein conformation. Further evidence for an apoAI-LPS specific interaction was obtained by incubation of the protein with 125I-ASD- LPS. The results show that multiple regions of the protein were able to interact with LPS, according to its amphiphatic nature. Finally, the contribution of the purified C-terminal fragment of the protein in the endotoxin neutralization was evaluated in comparison with the effect of apoAI. In both cases, the same decrease in tumor necrosis factor-α released was observed. This result suggests that the C-terminal half of apoAI is the main domain responsible of the neutralization effect of this protein. Our data may provide innovative pharmacological tools in endotoxin neutralization therapies.
format Articulo
Articulo
author Henning, María Florencia
Herlax, Vanesa Silvana
Bakás, Laura Susana
author_facet Henning, María Florencia
Herlax, Vanesa Silvana
Bakás, Laura Susana
author_sort Henning, María Florencia
title Contribution of the C-terminal end of apolipoprotein AI to neutralization of lipopolysaccharide endotoxic effect
title_short Contribution of the C-terminal end of apolipoprotein AI to neutralization of lipopolysaccharide endotoxic effect
title_full Contribution of the C-terminal end of apolipoprotein AI to neutralization of lipopolysaccharide endotoxic effect
title_fullStr Contribution of the C-terminal end of apolipoprotein AI to neutralization of lipopolysaccharide endotoxic effect
title_full_unstemmed Contribution of the C-terminal end of apolipoprotein AI to neutralization of lipopolysaccharide endotoxic effect
title_sort contribution of the c-terminal end of apolipoprotein ai to neutralization of lipopolysaccharide endotoxic effect
publishDate 2011
url http://sedici.unlp.edu.ar/handle/10915/83921
work_keys_str_mv AT henningmariaflorencia contributionofthecterminalendofapolipoproteinaitoneutralizationoflipopolysaccharideendotoxiceffect
AT herlaxvanesasilvana contributionofthecterminalendofapolipoproteinaitoneutralizationoflipopolysaccharideendotoxiceffect
AT bakaslaurasusana contributionofthecterminalendofapolipoproteinaitoneutralizationoflipopolysaccharideendotoxiceffect
bdutipo_str Repositorios
_version_ 1764820488190689280

Ejemplares similares